Direct interaction between adenovirus E1A protein and the TATA box binding transcription factor IID.

Horikoshi, Nobuo; Maguire, Kathleen A.; Kralli, Anastasia; Maldonado, Edio; Reinberg, Danny; Weinmann, Roberto

doi:10.1073/pnas.88.12.5124

Cited by 228 publications

(149 citation statements)

References 45 publications

(41 reference statements)

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“…The high sequence conservation suggests that the C-terminal region of the maize TFIID protein is also involved in specific reactions like TATA box binding and interactions with the general transcriptional machinery, as has been shown for yeast and human TFIIDs [20,. It is interesting to note that most of the differences lie in the central basic core region that has the potential to form an alpha-helix and might be involved in protein-protein interactions [23,30].…”

Section: Discussion Febsmentioning

confidence: 99%

Two different cDNAs encoding TFIID proteins of maize

Haaß

Feix

1992

FEBS Letters

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Two different complementary DNAs (cDNAs) encoding maize TFIID proleins were isolated from a maize IcafcDNA. Both cDNA sequences reveal two types ofTFIID. each encoding an open reading frame of 200 amino acids. The two cDNAs arc 76% identical a~ the DNA level and their putative amino acid sequences din'er at only three amino acids, Like TATA box binding proteins from other organisms they show a bipartite structure containing a spexilic N-terminal region and a highly conserved C-terminal domain expected to be necessary and suflicient for the essential TFIID functions in transcriptional initiation.Transcription initiation; TFIID; TATA box binding protein; ZL'N ~IUJ~S

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Section: Discussion Febsmentioning

confidence: 99%

Two different cDNAs encoding TFIID proteins of maize

Haaß

Feix

1992

FEBS Letters

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“…Moreover, proteins which modulate transcription interact with the C-terminal domain (15)(16)(17)(18)(19)(20)(21)(22). We investigated regions of the mouse TBP that are responsible for TBP multimerization.…”

Section: Multinerization Of Tbp In Solutionmentioning

confidence: 99%

“…Hence, TBP includes two characteristics: DNA (TATA-box) binding and protein binding. In contrast to ordinary transcription regulators, TBP can interact with a number of proteins such as TBPassociated factors consisting of SLI, TFIID and TFIIIB complexes (4)(5)(6)(7)(8)(9)(10), general transcription factors (TFIIB, TFIIA and a subunit of RNA polymerase 11) (11)(12)(13)(14), as well as transcription regulatory factors (sequence-specific DNA-binding proteins) and other regulators (15)(16)(17)(18)(19)(20)(21)(22).…”

Section: Introductionmentioning

confidence: 99%

Multimerization of the mouse TATA-binding protein (TBP) driven by its C-terminal conserved domain

Kato

Makino²,

Kishimoto³

et al. 1994

Nucl Acids Res

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The conformational states of the mouse TATA-binding protein (TBP) in solution were studied. A histidine tag and a factor Xa recognition site-carrying mouse TBP was expressed in E.coli, highly purified, and its fundamental functions as a TBP were demonstrated. We analyzed the molecular states of mouse TBP by gel filtration and glycerol gradient sedimentation, and found that TBP forms heterogeneous multimers in solution. Direct binding of TBP molecules to each other was proven by the far-Western procedure. Analyses using TBPs truncated at the N-and C-termini demonstrated that the functionally important C-terminal domain was responsible for homomultimer formation, and the N-terminal domain enhances multimerization. Furthermore, it was found that the TATA sequence dissociates homomultimers, and only monomeric TBP binds to the TATA-box. We suggest that TBP shares structural motifs in the C-terminal conserved domain for intermolecular interaction and TATA-binding.

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“…These include the highly acidic activation domains in VP16 (50,103), p53 (10,67,72,84,97,108), c-Myc (39), v-Rel and c-Rel (55,118), and E2F-1 (37), as well as other kinds of activation domains found in the adenovirus activator ElA (48,62), the Epstein-Barr virus proteins Zta (64) and R (70), the human T-cell leukemia virus type 1 (HTLV-1) activator Taxl (8), the transactivator Tat of human immunodeficiency virus type 1 (HIV-1) (53), and human c-Fos and c-Jun (85), PU-1 (38), and Spl (20). In certain cases, reduced binding of TBP by activation domains with point mutations that reduce transactivation in vivo has provided evidence for the biological relevance of these interactions (8,50,53,62).…”

mentioning

confidence: 99%

Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53.

Xiao¹,

Pearson²,

Coulombe³

et al. 1994

Mol. Cell. Biol.

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339

274

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Acidic transcriptional activation domains function well in both yeast and mammalian cells, and some have been shown to bind the general transcription factors TFIID and TFIIB. We now show that two acidic transactivators, herpes simplex virus VP16 and human p53, directly interact with the multisubunit human general transcription factor TFIHH and its Saccharomyces cerevisuze counterpart, factor b. The VP16-and p53-binding domains in these factors lie in the p62 subunit of TFIIH and in the homologous subunit, TFB1, of factor b. Point mutations in VP16 that reduce its transactivation activity in both yeast and mammalian cells weaken its binding to both yeast and human TFIIH. This suggests that binding of activation domains to TFIIH is an important aspect of transcriptional activation.Accurate transcription in vitro by human RNA polymerase II involves the general transcription factors TFIIA, TFIIB, TFIID, TFIIE, TFIIF (RAP30 and RAP74), TFIIH (also known as BTF2), and TFIIJ (reviewed in references 13 and 121). Beginning with TFIID, which recognizes the TATA boxes present in many promoters for RNA polymerase II, these factors and RNA polymerase II can be assembled in a defined order onto a promoter (5). TFIIH and TFIIJ are the last of these factors to bind to an assembling initiation complex (12,14,26), and TFIIH, also known as BTF2, is the only factor known to possess associated enzymatic activities. These include an ATP-dependent DNA helicase activity (95, 96) and a protein kinase activity that can phosphorylate the carboxyterminal heptapeptide repeat domain (CTD) of the largest subunit of RNA polymerase 11 (12, 21,68 herpes simplex virus transactivator VP16 (107) and in the N-terminal 73 amino acids of the mammalian tumor suppressor protein p53 (23). The p53 protein has a site-specific DNA-binding domain in its carboxy-terminal portion (101). VP16 does not, by itself, bind specifically to DNA, but instead its amino-terminal portion binds DNA in association with mammalian factors, including the POU homeodomain protein Oct-1 that recognizes octamer sequences in DNA (28,60,102). When fused to the DNA-binding domain of GAL4, the VP16 and p53 activation domains stimulate transcription in yeast and human cells of a gene bearing GAL4-binding sites (9,16,23,74,87,92). These observations imply that common mechanisms for transcriptional activation by acidic activators may exist in fungi and mammals.Many activation domains have been shown to interact with the TATA-box-binding protein (TBP) subunit of TFIID. These include the highly acidic activation domains in VP16 (50,103), p53 (10,67,72,84,97,108),118), and E2F-1 (37), as well as other kinds of activation domains found in the adenovirus activator ElA (48, 62), the Epstein-Barr virus proteins Zta (64) and R (70), the human T-cell leukemia virus type 1 (HTLV-1) activator Taxl (8), the transactivator Tat of human immunodeficiency virus type 1 (HIV-1) (53), and human c-Fos and c-Jun (85), PU-1 (38), and Spl (20). In certain cases, reduced binding of TBP by activation domains wit...

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Direct interaction between adenovirus E1A protein and the TATA box binding transcription factor IID.

Cited by 228 publications

References 45 publications

Two different cDNAs encoding TFIID proteins of maize

Two different cDNAs encoding TFIID proteins of maize

Multimerization of the mouse TATA-binding protein (TBP) driven by its C-terminal conserved domain

Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53.

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